The dynamical behavior of proteins will be investigated, using time-resolved Raman and infrared spectroscopies as probes of structure in real time. Laser temperature-jump techniques will be applied to the protein folding problem in order to characterize the earliest stages in folding and unfolding. T-jump studies will be extended to investigate protein motions tied to function: enzyme activity in alcohol dehydrogenase, iron release from ferritin, and apoptosis triggering by cytochrome c. The dynamics of protein allostery will be investigated, using hemoglobin as a paradigm. Pump-probe spectroscopic monitoring of the R-T conformation change will be used to define the reaction coordinate in molecular detail, using site-directed mutagenesis and metal substitution, in conjunction with computational modeling. By increasing our understanding of hemoglobin, these studies may lead to improved hematological therapies.